메뉴 건너뛰기




Volumn 5, Issue 10, 1999, Pages 439-447

p38 MAPK signalling cascades in inflammatory disease

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR;

EID: 0032850020     PISSN: 13574310     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-4310(99)01544-0     Document Type: Review
Times cited : (536)

References (44)
  • 1
    • 10744227768 scopus 로고    scopus 로고
    • Acquisition of sensitivity of stress-activated protein kinases to the p38 inhibitor, SB 203580, by alteration of one or more amino acids within the ATP binding pocket
    • R.J. Gum Acquisition of sensitivity of stress-activated protein kinases to the p38 inhibitor, SB 203580, by alteration of one or more amino acids within the ATP binding pocket J. Biol. Chem. 273 1998 15605 15610
    • (1998) J. Biol. Chem. , vol.273 , pp. 15605-15610
    • Gum, R.J.1
  • 2
    • 0033120590 scopus 로고    scopus 로고
    • Differential expression and activation of p38 mitogen-activated protein kinase α, β, γ and δ in inflammatory cell lineages
    • K.K. Hale D. Trollinger M. Rihanek C.L. Manthey Differential expression and activation of p38 mitogen-activated protein kinase α, β, γ and δ in inflammatory cell lineages J. Immunol. 162 1999 4246 4252
    • (1999) J. Immunol. , vol.162 , pp. 4246-4252
    • Hale, K.K.1    Trollinger, D.2    Rihanek, M.3    Manthey, C.L.4
  • 3
    • 0030868682 scopus 로고    scopus 로고
    • Kinetic mechanism for p38 MAP kinase
    • P.V. LoGrasso Kinetic mechanism for p38 MAP kinase Biochemistry 36 1997 10422 10427
    • (1997) Biochemistry , vol.36 , pp. 10422-10427
    • LoGrasso, P.V.1
  • 4
    • 0032519736 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or FMLP stimulation
    • Y.L. Zu p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or FMLP stimulation J. Immunol. 160 1998 1982 1989
    • (1998) J. Immunol. , vol.160 , pp. 1982-1989
    • Zu, Y.L.1
  • 5
    • 0030756286 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase
    • X.S. Wang Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase J. Biol. Chem. 272 1997 23668 23674
    • (1997) J. Biol. Chem. , vol.272 , pp. 23668-23674
    • Wang, X.S.1
  • 6
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • J.C. Lee A protein kinase involved in the regulation of inflammatory cytokine biosynthesis Nature 372 1994 739 746
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1
  • 7
    • 0031587929 scopus 로고    scopus 로고
    • Novel homologs of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles
    • S. Kumar Novel homologs of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles Biochem. Biophys. Res. Commun. 235 1997 533 538
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 533-538
    • Kumar, S.1
  • 8
    • 0030702895 scopus 로고    scopus 로고
    • A novel SAPK/JNK kinase, MKK7, stimulated by TNFα and cellular stresses
    • T. Moriguchi A novel SAPK/JNK kinase, MKK7, stimulated by TNFα and cellular stresses EMBO J. 16 1997 7045 7053
    • (1997) EMBO J. , vol.16 , pp. 7045-7053
    • Moriguchi, T.1
  • 9
    • 0032575591 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/erk kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38
    • T. Yuasa S. Ohno J.H. Kehrl J.M. Kyriakis Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/erk kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38 J. Biol. Chem. 273 1998 22681 22692
    • (1998) J. Biol. Chem. , vol.273 , pp. 22681-22692
    • Yuasa, T.1    Ohno, S.2    Kehrl, J.H.3    Kyriakis, J.M.4
  • 10
    • 0030805915 scopus 로고    scopus 로고
    • p38-2, a novel mitogen-activated protein kinase with distinct properties
    • B. Stein p38-2, a novel mitogen-activated protein kinase with distinct properties J. Biol. Chem. 272 1997 19509 19517
    • (1997) J. Biol. Chem. , vol.272 , pp. 19509-19517
    • Stein, B.1
  • 11
    • 0030927106 scopus 로고    scopus 로고
    • Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases
    • M. Goedert Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases EMBO J. 16 1997 3563 3571
    • (1997) EMBO J. , vol.16 , pp. 3563-3571
    • Goedert, M.1
  • 12
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • M. Deak A.D. Clifton J.M. Lucocq D.R. Alessi Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB EMBO J. 17 1998 4426 4441
    • (1998) EMBO J. , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, J.M.3    Alessi, D.R.4
  • 13
    • 0030588188 scopus 로고    scopus 로고
    • Activation of p38 in stimulated human neutrophils: phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK
    • J. El Benna Activation of p38 in stimulated human neutrophils: phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK Arch. Biochem. Biophys. 334 1996 395 400
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 395-400
    • El Benna, J.1
  • 15
    • 0030661712 scopus 로고    scopus 로고
    • Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated protein kinases in human neutrophils
    • K.I. Hidari A.S. Weyrich G.A. Zimmerman R.P. McEver Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated protein kinases in human neutrophils J. Biol. Chem. 272 1997 28750 28756
    • (1997) J. Biol. Chem. , vol.272 , pp. 28750-28756
    • Hidari, K.I.1    Weyrich, A.S.2    Zimmerman, G.A.3    McEver, R.P.4
  • 16
    • 0031018424 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced E-selectin expression is activated by the nuclear factor-κB and c-jun N-terminal kinase/p38 mitogen-activated protein kinase pathways
    • M.A. Read Tumor necrosis factor α-induced E-selectin expression is activated by the nuclear factor-κB and c-jun N-terminal kinase/p38 mitogen-activated protein kinase pathways J. Biol. Chem. 272 1997 2753 2761
    • (1997) J. Biol. Chem. , vol.272 , pp. 2753-2761
    • Read, M.A.1
  • 17
    • 0033559424 scopus 로고    scopus 로고
    • Selective activation and functional significance of p38α mitogen-activated protein kinase in lipopolysaccharide-stimulated neutrophils
    • J.A. Nick Selective activation and functional significance of p38α mitogen-activated protein kinase in lipopolysaccharide-stimulated neutrophils J. Clin. Invest. 103 1999 851 858
    • (1999) J. Clin. Invest. , vol.103 , pp. 851-858
    • Nick, J.A.1
  • 18
    • 85119798345 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase is a mechanism of priming in macrophages
    • G.J. Bauer I. Garcia R.V. Maier Activation of stress-activated protein kinase is a mechanism of priming in macrophages Surg. Forum 48 1997 43 45
    • (1997) Surg. Forum , vol.48 , pp. 43-45
    • Bauer, G.J.1    Garcia, I.2    Maier, R.V.3
  • 19
    • 0031114081 scopus 로고    scopus 로고
    • Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase. Regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels
    • S.H. Ridley Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase. Regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels J. Immunol. 158 1997 3165 3173
    • (1997) J. Immunol. , vol.158 , pp. 3165-3173
    • Ridley, S.H.1
  • 20
    • 0030048490 scopus 로고    scopus 로고
    • Interleukin-8 regulation of the Ras/Raf/mitogen-activated protein kinase pathway in human neutrophils
    • C. Knall Interleukin-8 regulation of the Ras/Raf/mitogen-activated protein kinase pathway in human neutrophils J. Biol. Chem. 271 1996 2832 2838
    • (1996) J. Biol. Chem. , vol.271 , pp. 2832-2838
    • Knall, C.1
  • 21
    • 0032529398 scopus 로고    scopus 로고
    • Role of stress-activated mitogen-activated protein kinase (p38) in β2-integrin-dependent neutrophil adhesion and the adhesion-dependent oxidative burst
    • P.A. Detmers Role of stress-activated mitogen-activated protein kinase (p38) in β2-integrin-dependent neutrophil adhesion and the adhesion-dependent oxidative burst J. Immunol. 161 1998 1921 1929
    • (1998) J. Immunol. , vol.161 , pp. 1921-1929
    • Detmers, P.A.1
  • 22
    • 0032562605 scopus 로고    scopus 로고
    • Two signaling mechanisms for activation of αMβ2 avidity in polymorphonuclear neutrophils
    • 2 avidity in polymorphonuclear neutrophils J. Biol. Chem. 273 1998 10556 10566
    • (1998) J. Biol. Chem. , vol.273 , pp. 10556-10566
    • Jones, S.L.1
  • 23
    • 0031550222 scopus 로고    scopus 로고
    • p38 mitogen activated protein kinase regulates endothelial VCAM-1 expression at the post-transcriptional level
    • A. Pietersma p38 mitogen activated protein kinase regulates endothelial VCAM-1 expression at the post-transcriptional level Biochem. Biophys. Res. Commun. 230 1997 44 48
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 44-48
    • Pietersma, A.1
  • 24
    • 0030903025 scopus 로고    scopus 로고
    • Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases
    • C. Knall G.S. Worthen G.L. Johnson Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases Proc. Natl. Acad. Sci. U. S. A. 94 1997 3052 3057
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3052-3057
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 25
    • 0032495987 scopus 로고    scopus 로고
    • The role of p38 MAP kinase in TGF-β1-induced signal transduction in human neutrophils
    • M. Hannigan L. Zhan Y. Ai C.K. Huang The role of p38 MAP kinase in TGF-β1-induced signal transduction in human neutrophils Biochem. Biophys. Res. Commun. 246 1998 55 58
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 55-58
    • Hannigan, M.1    Zhan, L.2    Ai, Y.3    Huang, C.K.4
  • 27
    • 0030937347 scopus 로고    scopus 로고
    • Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP
    • J.A. Nick Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP J. Clin. Invest. 99 1997 975 986
    • (1997) J. Clin. Invest. , vol.99 , pp. 975-986
    • Nick, J.A.1
  • 28
    • 85119793615 scopus 로고    scopus 로고
    • Role of p38 MAP kinase in human neutrophil priming for superoxide production and elastase release
    • D.A. Partrick Role of p38 MAP kinase in human neutrophil priming for superoxide production and elastase release Surg. Forum 48 1997 48 50
    • (1997) Surg. Forum , vol.48 , pp. 48-50
    • Partrick, D.A.1
  • 29
    • 0030827057 scopus 로고    scopus 로고
    • Tumor necrosis factor α and interleukin 1 signalling: do MAPKK kinases connect it all?
    • J. Eder Tumor necrosis factor α and interleukin 1 signalling: do MAPKK kinases connect it all? Trends Pharmacol. Sci. 18 1997 319 322
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 319-322
    • Eder, J.1
  • 30
    • 0032549174 scopus 로고    scopus 로고
    • IκBα degradation and nuclear factor κB DNA binding are insufficient for interleukin-1β and tumor necrosis factor-α-induced κB-dependent transcription. Requirement for an additional activation pathway
    • M. Bergmann IκBα degradation and nuclear factor κB DNA binding are insufficient for interleukin-1β and tumor necrosis factor-α-induced κB-dependent transcription. Requirement for an additional activation pathway J. Biol. Chem. 273 1998 6607 6610
    • (1998) J. Biol. Chem. , vol.273 , pp. 6607-6610
    • Bergmann, M.1
  • 31
    • 0030911732 scopus 로고    scopus 로고
    • Activation of transcription factor NFκB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways
    • S. Wesselborg Activation of transcription factor NFκB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways J. Biol. Chem. 272 1997 12422 12429
    • (1997) J. Biol. Chem. , vol.272 , pp. 12422-12429
    • Wesselborg, S.1
  • 32
    • 0030426902 scopus 로고    scopus 로고
    • Pharmacological profile of SB 203580, a selective inhibitor of cytokine suppressive binding protein/p38 kinase, in animal models of arthritis, bone resorption, endotoxin shock and immune function
    • A.M. Badger Pharmacological profile of SB 203580, a selective inhibitor of cytokine suppressive binding protein/p38 kinase, in animal models of arthritis, bone resorption, endotoxin shock and immune function J. Pharmacol. Exp. Ther. 279 1996 1453 1461
    • (1996) J. Pharmacol. Exp. Ther. , vol.279 , pp. 1453-1461
    • Badger, A.M.1
  • 33
    • 12644277392 scopus 로고    scopus 로고
    • The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase
    • K.P. Wilson The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase Chem. Biol. 4 1997 423 431
    • (1997) Chem. Biol. , vol.4 , pp. 423-431
    • Wilson, K.P.1
  • 34
    • 0030954172 scopus 로고    scopus 로고
    • A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket
    • L. Tong A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket Nat. Struct. Biol. 4 1997 311 316
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 311-316
    • Tong, L.1
  • 35
    • 0032530336 scopus 로고    scopus 로고
    • Structural basis of inhibitor selectivity in MAP kinases
    • Z. Wang Structural basis of inhibitor selectivity in MAP kinases Structure 6 1998 1117 1128
    • (1998) Structure , vol.6 , pp. 1117-1128
    • Wang, Z.1
  • 36
    • 0032578559 scopus 로고    scopus 로고
    • The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding
    • B. Frantz The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding Biochemistry 37 1998 13846 13853
    • (1998) Biochemistry , vol.37 , pp. 13846-13853
    • Frantz, B.1
  • 37
    • 0030924833 scopus 로고    scopus 로고
    • Pyridinyl imidazole inhibitors of p38 mitogen-activated protein kinase bind in the ATP site
    • P.R. Young Pyridinyl imidazole inhibitors of p38 mitogen-activated protein kinase bind in the ATP site J. Biol. Chem. 272 1997 12116 12121
    • (1997) J. Biol. Chem. , vol.272 , pp. 12116-12121
    • Young, P.R.1
  • 38
    • 0032564311 scopus 로고    scopus 로고
    • Molecular basis for p38 protein kinase inhibitor specificity
    • J.M. Lisnock Molecular basis for p38 protein kinase inhibitor specificity Biochemistry 37 1998 16573 16581
    • (1998) Biochemistry , vol.37 , pp. 16573-16581
    • Lisnock, J.M.1
  • 39
    • 0031934170 scopus 로고    scopus 로고
    • Pharmacological effects of SB 220025, a selective inhibitor of P38 mitogen-activated protein kinase, in angiogenesis and chronic inflammatory disease models
    • J.R. Jackson Pharmacological effects of SB 220025, a selective inhibitor of P38 mitogen-activated protein kinase, in angiogenesis and chronic inflammatory disease models J. Pharmacol. Exp. Ther. 284 1998 687 692
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 687-692
    • Jackson, J.R.1
  • 40
    • 0031765795 scopus 로고    scopus 로고
    • Conquering airway inflammation in the 21st century
    • D.F. Rogers M.A. Giembycz Conquering airway inflammation in the 21st century Drug Discov. Today 3 1998 532 535
    • (1998) Drug Discov. Today , vol.3 , pp. 532-535
    • Rogers, D.F.1    Giembycz, M.A.2
  • 41
    • 0028907221 scopus 로고
    • Molecular cloning of human p38 MAP kinase
    • J. Han Molecular cloning of human p38 MAP kinase Biochim. Biophys. Acta 1265 1995 224 227
    • (1995) Biochim. Biophys. Acta , vol.1265 , pp. 224-227
    • Han, J.1
  • 42
    • 0027994002 scopus 로고
    • An osmosensing signal transduction pathway in mammalian cells
    • Z. Galcheva-Gargova B. Derijard I.H. Wu R.J. Davis An osmosensing signal transduction pathway in mammalian cells Science 265 1994 806 808
    • (1994) Science , vol.265 , pp. 806-808
    • Galcheva-Gargova, Z.1    Derijard, B.2    Wu, I.H.3    Davis, R.J.4
  • 43
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38β)
    • Y. Jiang Characterization of the structure and function of a new mitogen-activated protein kinase (p38β) J. Biol. Chem. 271 1996 17920 17926
    • (1996) J. Biol. Chem. , vol.271 , pp. 17920-17926
    • Jiang, Y.1
  • 44
    • 0030581626 scopus 로고    scopus 로고
    • The primary structure of p38γ: a new member of p38 group of MAP kinases
    • Z. Li Y. Jiang R.J. Ulevitch J. Han The primary structure of p38γ: a new member of p38 group of MAP kinases Biochem. Biophys. Res. Commun. 228 1996 334 340
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 334-340
    • Li, Z.1    Jiang, Y.2    Ulevitch, R.J.3    Han, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.